cooperativity and allostery

Question 1

enzymes displaying cooperative substrate binding?

Question 2

A cooperative enzyme can generally adopt two different conformations of near equal stability, but with differing activities. These are described as the ‘Tense’ state, where the enzyme can be said to have Blank 1 affinity for the substrate, giving a higher Blank 2 and the ‘Relaxed’ state, where the enzyme can be said to have Blank 3 affinity for the substrate, giving a Blank 4 Km.

Question 3

In terms of relative substrate concentrations, what is the advantage of cooperative substrate binding?

Question 4

What term could describe a molecule which, on binding to an enzyme displaying cooperative binding kinetics, stabilises the ‘tense’ state?

Question 5

2,3-Bisphosphoglycerate is an allosteric inhibitor of what

Question 6

Oxygen is delivered to tissues by the protein Blank 1, this is a teramer and so displays Blank 2 substrate binding. The protein Blank 3 binds to oxyegn in cells and tissues and its structure is one of a Blank 4, meaning that it displays Michaelis Menten kinetics and a graph of rate vs substrate concentration would appear Blank 5.